Characterizing weak protein-protein complexes by NMR residual dipolar couplings.

TitleCharacterizing weak protein-protein complexes by NMR residual dipolar couplings.
Publication TypeJournal Article
Year of Publication2011
AuthorsRingkjøbing Jensen, M., J-L. Ortega-Roldan, L. Salmon, N. A. J. van Nuland, and M. Blackledge
JournalEur Biophys J
Volume40
Issue12
Pagination1371-81
Date Published2011 Dec
ISSN1432-1017
KeywordsMacromolecular Substances, Magnetic Resonance Spectroscopy, Molecular Dynamics Simulation, Protein Binding, Protein Structure, Tertiary, Proteins
Abstract

Protein-protein interactions occur with a wide range of affinities from tight complexes characterized by femtomolar dissociation constants to weak, and more transient, complexes of millimolar affinity. Many of the weak and transiently formed protein-protein complexes have escaped characterization due to the difficulties in obtaining experimental parameters that report on the complexes alone without contributions from the unbound, free proteins. Here, we review recent developments for characterizing the structures of weak protein-protein complexes using nuclear magnetic resonance spectroscopy with special emphasis on the utility of residual dipolar couplings.

DOI10.1007/s00249-011-0720-5
Alternate JournalEur. Biophys. J.
PubMed ID21710303